cDNA Clones for Corn Leaf NADH:Nitrate Reductase and Chloroplast NAD(P)<sup>+</sup>:Glyceraldehyde-3-Phosphate Dehydrogenase

Gowri, G.; Campbell, Wilbur H.

doi:10.1104/pp.90.3.792

Cited by 87 publications

(29 citation statements)

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“…Corn Nir was found to be encoded by a very different set of codons than the Nir gene of spinach (2,17). We found that corn Nar codon usage was narrowly biased as compared to a Nar gene of Arabidopsis (10,13). A recent study of 207 plant genes confirmed that codon usage in nuclear genes differed between monocots and dicots (22).…”

mentioning

confidence: 64%

“…However, the high-level expression of the highly biased genes of monocots in the dicot system may be a problem. Genes such as Nar and Nir of corn as well as the corn chloroplastic Gap (8,13,17,28) may be very useful for experimentally testing the limits ofintergenic transfer in order to gain a better understanding ofbiased codon usage in higher plants.…”

Section: Significance Of Biased Codon Usage In Higher Plantsmentioning

confidence: 99%

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Codon Usage in Higher Plants, Green Algae, and Cyanobacteria

Campbell

Gowri²

1990

Plant Physiol.

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222

107

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Codon usage is the selective and nonrandom use of synonymous codons by an organism to encode the amino acids in the genes for its proteins. During the last few years, a large number of plant genes have been cloned and sequenced, which now permits a meaningful comparison of codon usage in higher plants, algae, and cyanobacteria. For the nuclear and organellar genes of these organisms, a small set of preferred codons are used for encoding proteins. Codon usage is different for each genome type with the variation mainly occurring in choices between codons ending in cytidine (C) or guanosine (G) versus those ending in adenosine (A) or uridine (U). For organellar genomes, chloroplastic and mitochrondrial proteins are encoded mainly with codons ending in A or U. In most cyanobacteria and the nuclei of green algae, proteins are encoded preferentially with codons ending in C or G. Although only a few nuclear genes of higher plants have been sequenced, a clear distinction between Magnoliopsida (dicot) and Liliopsida (monocot) codon usage is evident. Dicot genes use a set of 44 preferred codons with a slight preference for codons ending in A or U. Monocot codon usage is more restricted with an average of 38 codons preferred, which are predominantly those ending in C or G. But two classes of genes can be recognized in monocots. One set of monocot genes uses codons similar to those in dicots, while the other genes are highly biased toward codons ending in C or G with a pattem similar to nuclear genes of green algae. Codon usage is discussed in relation to evolution of plants and prospects for intergenic transfer of particular genes.

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mentioning

confidence: 64%

Section: Significance Of Biased Codon Usage In Higher Plantsmentioning

confidence: 99%

Codon Usage in Higher Plants, Green Algae, and Cyanobacteria

Campbell

Gowri²

1990

Plant Physiol.

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222

107

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“…Flavodoxin reductase arginine residues 144, 174 and 184 are highlighted in bold, as are positively charged amino acids (arginines and lysines) conserved in the aligned enzymes. Spinach, spinach FNR (Swiss-Prot code P00455, [24]) ; Anabaena, ferredoxin reductase from Anabaena variabilis (Q4459) ; P450 BM3, flavocytochrome P450 BM3 from Bacillus megaterium (P14779, [25]) ; Hum CPR, human NADPH-cytochrome P450 reductase (P16435, [26]) ; Rat CPR, rat NADPH-cytochrome P450 reductase (P00388, [27]) ; B5 R 'ASE, bovine NADH-cytochrome b 5 reductase (P07514, [28]) ; Hum iNOS, human inducible nitric oxide synthase (NOS ; P35228, [29]) ; Hum nNOS, human neuronal NOS (P29475, [30]) ; Hum eNOS, human endothelial NOS (P29474, [31]) ; Corn NIR, corn nitrate reductase (P17571, [32]). Bovine cytochrome b 5 reductase and corn nitrate reductase are NADH-dependent reductases, all other enzymes shown are NADPH-dependent.…”

Section: Discussionmentioning

confidence: 99%

Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase

Leadbeater

McIver

Campopiano

et al. 2000

Biochemical Journal

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The structure of the Escherichia coli flavodoxin NADP + oxidoreductase (FLDR) places three arginines (R144, R174 and R184) in the proposed NADPH-binding site. Mutant enzymes produced by site-directed mutagenesis, in which each arginine was replaced by neutral alanine, were characterized. All mutants exhibited decreased NADPH-dependent cytochrome c reductase activity (R144A, 241.6 min V " ; R174A, 132.1 min V " ; R184A, 305.5 min V " versus wild type, 338.9 min V ") and increased K m for NADPH (R144A, 5.3 µM ; R174A, 20.2 µM ; R184A, 54.4 µM versus wild type, 3.9 µM). The k cat value for NADH-dependent cytochrome c reduction was increased for R174A (42.3 min V ") and R184A (50.4 min V ") compared with the wild type (33.0 min V "), consistent with roles for R174 and R184 in discriminating between NADPH\NADH by interaction with the adenosine ribose 2h-phosphate. Stopped-flow studies indicated that affinity (K d ) for NADPH was markedly reduced in mutants R144A (635 µM) and R184A (2.3 mM) compared with the wild

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“…Total RNA was fractionated (10 rglsample) in formaldehyde-agarose denaturing gels by electrophoresis and transferred to nitrocellulose. Maize NR mRNA levels were probed by hybridization with a 32P-labeled cDNA clone of the maize NR mRNA (Gowri and Campbell, 1989) as previously described (Redinbaugh et al, 1988;Gowri et al, 1992). Briefly, a nonspecifically bound probe was eliminated by washing the membrane in 0.1 X SSC (0.15 m~ Na-citrate, pH 7.0, 15 m~ NaC1, 0.1% [w/v] SDS) at 65OC for at least 1 h. The Zmnrl cDNA hybridized with an mRNA of about 3.2 kb as previously seen (Gowri and Campbell, 1989).…”

Section: Rna Isolation and Northern Blot Analysis Of Nr Rnrnamentioning

confidence: 99%

Regulation of Maize Leaf Nitrate Reductase Activity Involves Both Gene Expression and Protein Phosphorylation

et al. 1994

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Nitrate reductase (NR; EC 1.6.6.1) activity increased at the beginning of the photoperiod in mature green maize (rea mays l.) leaves as a result of increased enzyme protein level and protein dephosphorylation. In vitro experiments suggested that phosphorylation of maize leaf NR affected sensitivity to Mgz* inhibition, as shown previously in spinach. When excised leaves were fed 32P-labeled inorganic phosphate, NR was phosphorylated on seryl residues in both the light and dark. Tryptic peptide mapping of NR labeled in vivo indicated three major 3ZP-phosphopeptide fragments, and labeling of all three was reduced when leaves were illuminated. Maize leaf NR mRNA levels that were low at the end of the dark period peaked within 2 h in the light and decreased thereafter, and NR activity generally remained high. It appears that light signals, rather than an endogenous rhythm, account primarily for diurnal variations in NR mRNA levels. Overall, regulation of NR activity in mature maize leaves in response to light signals appears to involve control of gene expression, enzyme protein synthesis, and reversible protein phosphorylation.

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cDNA Clones for Corn Leaf NADH:Nitrate Reductase and Chloroplast NAD(P)⁺:Glyceraldehyde-3-Phosphate Dehydrogenase

Abstract: cDNA clones were selected from a corn (Zea mays L.) leaf lambda gtl1 expression library using polyclonal antibodies for corn leaf NADH:nitrate reductase. One clone, Zmnrl, had a 2

Cited by 87 publications

References 14 publications

Codon Usage in Higher Plants, Green Algae, and Cyanobacteria

Codon Usage in Higher Plants, Green Algae, and Cyanobacteria

Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase

Regulation of Maize Leaf Nitrate Reductase Activity Involves Both Gene Expression and Protein Phosphorylation

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cDNA Clones for Corn Leaf NADH:Nitrate Reductase and Chloroplast NAD(P)+:Glyceraldehyde-3-Phosphate Dehydrogenase

Abstract: cDNA clones were selected from a corn (Zea mays L.) leaf lambda gtl1 expression library using polyclonal antibodies for corn leaf NADH:nitrate reductase. One clone, Zmnrl, had a 2

Cited by 87 publications

References 14 publications

Codon Usage in Higher Plants, Green Algae, and Cyanobacteria

Codon Usage in Higher Plants, Green Algae, and Cyanobacteria

Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase

Regulation of Maize Leaf Nitrate Reductase Activity Involves Both Gene Expression and Protein Phosphorylation

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Product

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cDNA Clones for Corn Leaf NADH:Nitrate Reductase and Chloroplast NAD(P)⁺:Glyceraldehyde-3-Phosphate Dehydrogenase